1. Technical Field
This disclosure relates generally compositions formulated to accelerate the production of collagen proteins with an animal. More particularly, this disclosure relates to compositions formulated to accelerate the production of collagen-containing tissues of an animal that contain the collagen proteins.
2. Description of the Related Art
At least 12 different types of collagen exist within an animal's body, with Type I collagen being the most abundant. The basic triple-helix structure of Type I collagen is the prototype for most of the other collagen types. The other types of collagen differ from Type I collagen in the length of their triple helix and the presence or absence of globular domains at their amino or carboxyl terminal ends. Collagen itself is made up of a unique Amino Acid (AA) and Imino Acid (IA) composition with 33% of the total residues being glycine (Gly), 10% proline (Pro), 10% hydroxyproline (Hyp), and about 1% hydroxylysine (Hyl).
The basic structural unit of all types of collagen is tropocollagen, which is cross-linked to from large fibers of collagenous tissues. Tropocollagen is made of three polypeptide chains called α chains, where each of the α chains is wound around the other to form a triple helix structure. Every third AA or IA in the α chain is a glycine (hence the value of 33% for the relative amount of glycine present in collagen).
Sixty percent of the α chains are made of either the sequence Gly-Pro-X or the sequence Gly-X-Hyp, where X may be any AA or IA. The remaining forty percent of the α chains are various sequences of AAs and IAs, with every third AA or IA being a glycine. The AAs and IAs that compose tropocollagen may be referred to as tropocollagen factors.
A subset of particular proline and lysine residues in the region where the triple-helix formation occurs are hydroxylated before assembly can take place. Three enzymes are required for proper hydroxylation: lysl hydroxylase, prolyl-4-hydroxylase, and prolyl-3-hydroxylase.
Lysl hydroxylase converts lysines in the sequence X-Lys-Gly to 5-hydroxylysine. Prolyl-4-hydroxylase converts prolines in the sequence X-Pro-Gly to 4-hydroxyproline. Prolyl-3-hydroxylase converts prolines in the sequence Hyp-Pro-Gly to 3-hydroxyproline. The above hydroxylation reactions require ferrous/ferric iron, ascorbic acid (vitamin C), oxygen, and α-ketoglutarate in the chemical reaction that is described below in equation (1).AA or IA residue+iron+ascorbic acid+O2+α-ketoglutarate→hydroxyl-AA or IA+succinate  (1)
Since the presence of new collagen proteins encourages the production of new collagen-containing tissues (e.g., cartilage tissue, tendon tissue, ligament tissue, hair tissue, etc.), the present inventor has found that it would be advantageous to develop compositions formulated to accelerate the production of new collagen proteins within an animal.